EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Visualizing chaperonin function in situ by cryo-electron tomography.
ジャーナル・号・ページ	Nature, Vol. 633, Issue 8029, Page 459-464, Year 2024
掲載日	2024年8月21日
著者	Jonathan Wagner / Alonso I Carvajal / Andreas Bracher / Florian Beck / William Wan / Stefan Bohn / Roman Körner / Wolfgang Baumeister / Ruben Fernandez-Busnadiego / F Ulrich Hartl /
PubMed 要旨	Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein folding. The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein and the lid-shaped cofactor ...Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein folding. The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein and the lid-shaped cofactor GroES at their apertures. In vitro analyses of the chaperonin reaction have shown that substrate protein folds, unimpaired by aggregation, while transiently encapsulated in the GroEL central cavity by GroES. To determine the functional stoichiometry of GroEL, GroES and client protein in situ, here we visualized chaperonin complexes in their natural cellular environment using cryo-electron tomography. We find that, under various growth conditions, around 55-70% of GroEL binds GroES asymmetrically on one ring, with the remainder populating symmetrical complexes. Bound substrate protein is detected on the free ring of the asymmetrical complex, defining the substrate acceptor state. In situ analysis of GroEL-GroES chambers, validated by high-resolution structures obtained in vitro, showed the presence of encapsulated substrate protein in a folded state before release into the cytosol. Based on a comprehensive quantification and conformational analysis of chaperonin complexes, we propose a GroEL-GroES reaction cycle that consists of linked asymmetrical and symmetrical subreactions mediating protein folding. Our findings illuminate the native conformational and functional chaperonin cycle directly within cells.
リンク	Nature / PubMed:39169181 / PubMed Central
手法	EM (単粒子) / EM (サブトモグラム平均)
解像度	2.5 - 15.2 Å
構造データ	17418 8p4m EMDB-17418, PDB-8p4m: CryoEM structure of a C7-symmetrical GroEL7-GroES7 cage in presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 2.5 Å 17420 8p4n EMDB-17420, PDB-8p4n: CryoEM structure of a GroEL7-GroES7 cage with encapsulated disordered substrate MetK in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 2.9 Å 17421 8p4o EMDB-17421, PDB-8p4o: CryoEM structure of a GroEL7-GroES7 cage with encapsulated ordered substrate MetK in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 3.04 Å EMDB-17422: Density for MetK encapsulated in the GroEL7-GroES7 cage 手法: EM (単粒子) / 解像度: 3.7 Å EMDB-17423: Symmetry-averaged GroEL7-GroES7 chamber with encapsulated disordered substrate MetK obtained by in vitro cryo electron tomography 手法: EM (サブトモグラム平均) / 解像度: 7.6 Å EMDB-17424: Symmetry-averaged GroEL7-GroES7 chamber with encapsulated ordered substrate MetK obtained by in vitro cryo electron tomography 手法: EM (サブトモグラム平均) / 解像度: 8.0 Å 17425 8p4p EMDB-17425, PDB-8p4p: Structure average of GroEL14 complexes found in the cytosol of Escherichia coli overexpressing GroEL obtained by cryo electron tomography 手法: EM (サブトモグラム平均) / 解像度: 9.6 Å 17426 8p4r EMDB-17426, PDB-8p4r: In situ structure average of GroEL14-GroES14 complexes in Escherichia coli cytosol obtained by cryo electron tomography 手法: EM (サブトモグラム平均) / 解像度: 11.9 Å EMDB-17534: Cryo-EM structure of a D7-symmetrical GroEL14-GroES14 complex in presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 2.74 Å EMDB-17535: Cryo-EM structure of a C7-symmetrical GroEL14-GroES7 complex in presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 2.66 Å EMDB-17559: In situ structure average of GroEL7-GroES7 chamber with no or disordered substrate in Escherichia coli cytosol obtained by cryo electron tomography 手法: EM (サブトモグラム平均) / 解像度: 15.1 Å EMDB-17560: In situ structure average of GroEL7-GroES7 chamber with encapsulated, ordered substrate in Escherichia coli cytosol obtained by cryo electron tomography 手法: EM (サブトモグラム平均) / 解像度: 15.2 Å EMDB-17561: Cryo-ET subtomogram of 70S ribosomes in Escherichia coli cells at 37 and 46 degrees centigrade and in Escherichia coli cells overexpressing GroELS and MetK 手法: EM (サブトモグラム平均) / 解像度: 8.4 Å EMDB-17562: Cryo-ET subtomogram of 70S ribosomes in Escherichia coli cells overexpressing GroEL 手法: EM (サブトモグラム平均) / 解像度: 6.3 Å EMDB-17563: CryoEM structure of a GroEL14-GroES7 cage with encapsulated ordered substrate MetK in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 3.47 Å EMDB-17564: CryoEM structure of a GroEL14-GroES7 cage with encapsulated disordered substrate MetK in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 3.22 Å EMDB-17565: CryoEM structure of a GroEL14-GroES14 cage with two encapsulated disordered MetK substrates in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 3.22 Å EMDB-17566: CryoEM structure of a (GroEL)14-(GroES)14 complex with encapsulated ordered MetK substrate in one chamber and no or disordered MetK substrate in the other chamber in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 3.15 Å EMDB-17567: Conformer 1 of the (GroEL)14(GroES)14 complex with two encapsulated, ordered and near-native MetK substrate molecules in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 4.5 Å EMDB-17568: Conformer 2 of the (GroEL)14(GroES)14 complex with two encapsulated, near-native and ordered MetK substrates in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 4.4 Å EMDB-17569: Conformer 3 of the (GroEL)14(GroES)14 complex with two encapsulated, near-native and ordered MetK substrates in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 4.4 Å EMDB-17570: Conformer 4 of the (GroEL)14(GroES)14 complex with two encapsulated, near-native and ordered MetK substrates in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 4.4 Å EMDB-17571: Conformer 5 of the (GroEL)14(GroES)14 complex with two encapsulated, near-native and ordered MetK substrates in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 4.7 Å EMDB-17572: Conformer 6 of the (GroEL)14(GroES)14 complex with two encapsulated, near-native and ordered MetK substrates in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 4.4 Å EMDB-17573: Conformer 7 of the (GroEL)14(GroES)14 complex with two encapsulated, near-native and ordered MetK substrates in the presence of ADP-BeFx 手法: EM (単粒子) / 解像度: 4.4 Å 18735 8qxs EMDB-18735, PDB-8qxs: CryoEM structure of a GroEL14-GroES7 complex in presence of ADP-BeFx with wide GroEL7 trans ring conformation 手法: EM (単粒子) / 解像度: 3.12 Å 18736 8qxt EMDB-18736, PDB-8qxt: CryoEM structure of a GroEL14-GroES7 complex in presence of ADP-BeFx with narrow GroEL7 trans ring conformation 手法: EM (単粒子) / 解像度: 2.9 Å 18737 8qxu EMDB-18737, PDB-8qxu: In situ structure average of GroEL14-GroES7 complexes with wide GroEL7 trans ring conformation in Escherichia coli cytosol obtained by cryo electron tomography 手法: EM (サブトモグラム平均) / 解像度: 12.0 Å 18738 8qxv EMDB-18738, PDB-8qxv: In situ structure average of GroEL14-GroES7 complexes with narrow GroEL7 trans ring conformation in Escherichia coli cytosol obtained by cryo electron tomography 手法: EM (サブトモグラム平均) / 解像度: 13.6 Å
化合物	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-BEF: BERYLLIUM TRIFLUORIDE ION ChemComp-K: Unknown entry / カリウムカチオン ChemComp-HOH: WATER ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM
由来	escherichia coli (大腸菌) escherichia coli bl21(de3) (大腸菌)
キーワード	CHAPERONE / Chaperonin / Folding cage / proteostasis / heat shock / ATPase